IL10H_HCMVA
ID IL10H_HCMVA Reviewed; 175 AA.
AC P17150; Q7M6T2; Q9J7C4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 29-SEP-2021, entry version 104.
DE RecName: Full=Viral interleukin-10 homolog;
DE Short=cmvIL-10;
DE Short=vIL-10;
DE Flags: Precursor;
GN Name=UL111A;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10677520; DOI=10.1073/pnas.97.4.1695;
RA Kotenko S.V., Saccani S., Izotova L.S., Mirochnitchenko O.V., Pestka S.;
RT "Human cytomegalovirus harbors its own unique interleukin-10 homolog
RT (cmvIL-10).";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1695-1700(2000).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP FUNCTION.
RX PubMed=15280480; DOI=10.1128/jvi.78.16.8720-8731.2004;
RA Chang W.L., Baumgarth N., Yu D., Barry P.A.;
RT "Human cytomegalovirus-encoded interleukin-10 homolog inhibits maturation
RT of dendritic cells and alters their functionality.";
RL J. Virol. 78:8720-8731(2004).
RN [6]
RP FUNCTION.
RX PubMed=19524994; DOI=10.1016/j.virol.2009.05.013;
RA Chang W.L., Barry P.A., Szubin R., Wang D., Baumgarth N.;
RT "Human cytomegalovirus suppresses type I interferon secretion by
RT plasmacytoid dendritic cells through its interleukin 10 homolog.";
RL Virology 390:330-337(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 20-175 IN COMPLEX WITH HUMAN
RP IL10R1, AND DISULFIDE BONDS.
RX PubMed=12093920; DOI=10.1073/pnas.152147499;
RA Jones B.C., Logsdon N.J., Josephson K., Cook J., Barry P.A., Walter M.R.;
RT "Crystal structure of human cytomegalovirus IL-10 bound to soluble human
RT IL-10R1.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9404-9409(2002).
CC -!- FUNCTION: Functional viral IL-10 homolog. Can bind to the human IL-10
CC receptor and compete with human IL-10 for binding sites. Requires both
CC subunits of the human IL-10 receptor complex to induce signal
CC transduction events and biological activities. IL-10 signaling pathway
CC has several immunosuppressive activities that are exploited by the
CC virus. Inhibits TLR-induced type I interferon production in host
CC plasmacytoid dendritic cells. {ECO:0000269|PubMed:15280480,
CC ECO:0000269|PubMed:19524994}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:12093920}.
CC -!- INTERACTION:
CC P17150; Q13651: IL10RA; Xeno; NbExp=2; IntAct=EBI-1033736, EBI-1031656;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35350.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X17403; CAA35350.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF182315; AAF36285.1; -; mRNA.
DR EMBL; BK000394; DAA00102.1; -; Genomic_DNA.
DR PIR; S09878; S09878.
DR PDB; 1LQS; X-ray; 2.70 A; L/M=20-167.
DR PDBsum; 1LQS; -.
DR SMR; P17150; -.
DR DIP; DIP-36823N; -.
DR IntAct; P17150; 1.
DR EvolutionaryTrace; P17150; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0039673; P:evasion by virus of host dendritic cell activity; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.10; -; 1.
DR Gene3D; 4.10.340.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR020443; IL-10/19/20/22/24/26_fam.
DR InterPro; IPR012352; IL-10_add_hlx.
DR InterPro; IPR020423; IL-10_CS.
DR Pfam; PF00726; IL10; 1.
DR SMART; SM00188; IL10; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00520; INTERLEUKIN_10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Disulfide bond;
KW Evasion of host immunity by viral interleukin-like protein; Glycoprotein;
KW Host-virus interaction; Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Modulation of host dendritic cell activity by virus; Reference proteome;
KW Secreted; Signal; Viral immunoevasion.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..175
FT /note="Viral interleukin-10 homolog"
FT /id="PRO_0000015378"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 37..127
FT /evidence="ECO:0000269|PubMed:12093920"
FT DISULFID 78
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:12093920"
FT DISULFID 81..132
FT /evidence="ECO:0000269|PubMed:12093920"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:1LQS"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:1LQS"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:1LQS"
SQ SEQUENCE 175 AA; 20007 MW; 2C3545486AC4A811 CRC64;
MLSVMVSSSL VLIVFFLGAS EEAKPATTTI KNTKPQCRPE DYATRLQDLR VTFHRVKPTL
QREDDYSVWL DGTVVKGCWG CSVMDWLLRR YLEIVFPAGD HVYPGLKTEL HSMRSTLESI
YKDMRQCPLL GCGDKSVISR LSQEAERKSD NGTRKGLSEL DTLFSRLEEY LHSRK
